|
Name |
Accession |
Description |
Interval |
E-value |
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
45-507 |
0e+00 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 1018.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 45 TYKTVAGVNGPLVILDQVKFPRYAEIVHLTLPDGTKRSGQVLEVTGSKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 124
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 125 DMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQ 204
Cdd:TIGR01040 81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 205 ICRQAGLVKKS-KDVMDYSEDNFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLVNDPTIERIITPRLALTSAEF 283
Cdd:TIGR01040 161 ICRQAGLVKLPtKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 284 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITRP 363
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 364 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 443
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33504537 444 TSDDLLYLEFLQKFERNFISQGAYENRTVFETLDIGWQLLRIFPKEMLKRIPQSTLAEFYPRDS 507
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKS 464
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
42-505 |
0e+00 |
|
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 440770 [Multi-domain] Cd Length: 462 Bit Score: 831.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 42 PRLTYKTVAGVNGPLVILDQVKFPRYAEIVHLTLPDGTKRSGQVLEVTGSKAVVQVFEGTSGIDAKKTTCEFTGDILRTP 121
Cdd:COG1156 2 MKKEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 122 VSEDMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEI 201
Cdd:COG1156 82 VSEDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 202 AAQICRQAGLVKkskdvmdySEDNFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLVNDPTIERIITPRLALTSA 281
Cdd:COG1156 162 AAQIARQAKVRG--------EEEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 282 EFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDIT 361
Cdd:COG1156 234 EYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDIT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 362 RPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEE 441
Cdd:COG1156 314 HPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33504537 442 ALTSDDLLYLEFLQKFERNFISQGAYENRTVFETLDIGWQLLRIFPKEMLKRIPQSTLAEFYPR 505
Cdd:COG1156 394 ALSETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPK 457
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
46-508 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 807.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 46 YKTVAGVNGPLVILDQVKFPRYAEIVHLTLPDGTKRSGQVLEVTGSKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSED 125
Cdd:PRK04196 4 YRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPVSED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 126 MLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQI 205
Cdd:PRK04196 84 MLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 206 CRQAGLVKkskdvmdySEDNFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLVNDPTIERIITPRLALTSAEFLA 285
Cdd:PRK04196 164 ARQAKVLG--------EEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 286 YQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITRPIP 365
Cdd:PRK04196 236 FEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITHPIP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 366 DLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALTS 445
Cdd:PRK04196 316 DLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEALSE 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33504537 446 DDLLYLEFLQKFERNFISQGAYENRTVFETLDIGWQLLRIFPKEMLKRIPQSTLAEFYPRDSK 508
Cdd:PRK04196 396 RDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRG 458
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
117-406 |
0e+00 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 610.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 117 ILRTPVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGL 196
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 197 PHNEIAAQICRQAGLVKkskdvmdySEDNFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLVNDPTIERIITPRL 276
Cdd:cd01135 81 PHNELAAQIARQAGVVG--------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 277 ALTSAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMP 356
Cdd:cd01135 153 ALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 33504537 357 NDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG 406
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
46-509 |
4.11e-118 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 354.34 E-value: 4.11e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 46 YKTVAGVNGPLVILdQVKFPRYAEIVHLTLPDGTKRSgQVLEVTGSKAVVQVFEGTSGI--DAKKTtceFTGDILRTPVS 123
Cdd:PRK02118 5 YTKITDITGNVITV-EAEGVGYGELATVERKDGSSLA-QVIRLDGDKVTLQVFGGTRGIstGDEVV---FLGRPMQVTYS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 124 EDMLGRVFNGSGKPIDRGPAvLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAA 203
Cdd:PRK02118 80 ESLLGRRFNGSGKPIDGGPE-LEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 204 QICRQAglvkkSKDVmdysednfaIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLVNDPTIERIITPRLALTSAEF 283
Cdd:PRK02118 159 RIALQA-----EADI---------IILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 284 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrNGSITQIPILTMPNDDITRP 363
Cdd:PRK02118 225 FALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVTHP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 364 IPDLTGYITEGQIYvdrqLHNRQIYPpinvLPSLSRLMKSAIGEgMTRKDHSDVSN---QLYACYAIGKDVQAMkavvGE 440
Cdd:PRK02118 304 VPDNTGYITEGQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM----GF 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33504537 441 EaLTSDDLLYLEFLQKFERNFISQGAyeNRTVFETLDIGWQLL-RIF-PKEMLkrIPQSTLAEFYPRDSKH 509
Cdd:PRK02118 371 K-LSNWDEKLLKFSELFESRLMDLEV--NIPLEEALDLGWKILaQCFhPEEVG--IKEQLIDKYWPKNCLH 436
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
172-398 |
1.49e-106 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 316.61 E-value: 1.49e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 172 GISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvkkSKDVmdysednfaIVFAAMGVNMETARFFKSDFEENG 251
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQA-----SADV---------VVYALIGERGREVREFIEELLGSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 252 SMDNVCLFLNLVNDPTIERIITPRLALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLA 331
Cdd:pfam00006 67 ALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33504537 332 TIYERAGRVEGRNGSITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLS 398
Cdd:pfam00006 146 RLLERAGRVKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
119-400 |
1.11e-102 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 309.00 E-value: 1.11e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 119 RTPVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPH 198
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 199 NEIAAQICRQAGlvkkskdvmdySEDNFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLVNDPTIERIITPRLAL 278
Cdd:cd19476 81 TVLAMQLARNQA-----------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 279 TSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPND 358
Cdd:cd19476 150 TIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 33504537 359 DITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 400
Cdd:cd19476 229 DLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_V_A-type_beta_C |
cd18112 |
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 ... |
408-502 |
2.22e-62 |
|
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349747 [Multi-domain] Cd Length: 95 Bit Score: 198.43 E-value: 2.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 408 GMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFERNFISQGAYENRTVFETLDIGWQLLRIFP 487
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 33504537 488 KEMLKRIPQSTLAEF 502
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
119-400 |
3.11e-44 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 156.95 E-value: 3.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 119 RTPVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPH 198
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 199 NEIAAQICRQAGlvkksKDVmdysednfaIVFAAMGvnmETAR----FFKSDFEENGsMDNVCLFLNLVNDPTIERIITP 274
Cdd:cd01136 81 STLLGMIARNTD-----ADV---------NVIALIG---ERGRevreFIEKDLGEEG-LKRSVLVVATSDESPLLRVRAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 275 RLALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQIPILT 354
Cdd:cd01136 143 YTATAIAEYFRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTVL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 33504537 355 MPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 400
Cdd:cd01136 220 VEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
69-401 |
2.54e-38 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 145.17 E-value: 2.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 69 EIVHLTLPDGTKRSGQVLEVTGSKAVVQVFEGTSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPAVLAED 148
Cdd:COG1157 42 ELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGI-SPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 149 YLDIMGQPINPQCR--IypEEMIQTGISAIDGMNSIARGQKIPIFSAAG------LphneiaAQICRQA-------GLV- 212
Cdd:COG1157 121 RRPLDAPPPNPLERarI--TEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstlL------GMIARNTeadvnviALIg 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 213 KKSKDVMDYSEDNF-------AIVFAAmgvnmeTarffkSDfeengsmdnvclflnlvnDPTIERIITPRLALTSAEFLA 285
Cdd:COG1157 193 ERGREVREFIEDDLgeeglarSVVVVA------T-----SD------------------EPPLMRLRAAYTATAIAEYFR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 286 YQcEKHVLVIltdMSS---YAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQI-PILTmPNDDIT 361
Cdd:COG1157 244 DQ-GKNVLLL---MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKGSITAFyTVLV-EGDDMN 316
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 33504537 362 RPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 401
Cdd:COG1157 317 DPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM 356
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
114-476 |
7.40e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 144.12 E-value: 7.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 114 TGDILRTPVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSA 193
Cdd:PRK06936 91 TGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 194 AGLPHNEIAAQICRQAglvkkSKDVmdysednfaIVFAAMGV-NMETARFFKSDFEENGsMDNVCLFLNLVNDPTIERII 272
Cdd:PRK06936 171 AGGGKSTLLASLIRSA-----EVDV---------TVLALIGErGREVREFIESDLGEEG-LRKAVLVVATSDRPSMERAK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 273 TPRLALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGrvEGRNGSITQIPI 352
Cdd:PRK06936 236 AGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSDKGSITALYT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 353 LTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGegmtrKDHSDVSNQLYACYAIGKDVQ 432
Cdd:PRK06936 313 VLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVS-----KEHKTWAGRLRELLAKYEEVE 387
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 33504537 433 AMkAVVGEEALTSDDLLYlEFLQKFE--RNFISQGAYENRTVFETL 476
Cdd:PRK06936 388 LL-LQIGEYQKGQDKEAD-QAIERIGaiRGFLRQGTHELSHFNETL 431
|
|
| ATP-synt_V_A-type_beta_N |
cd18118 |
V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 ... |
45-116 |
8.23e-38 |
|
V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core, that is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex which forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349742 [Multi-domain] Cd Length: 72 Bit Score: 132.94 E-value: 8.23e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33504537 45 TYKTVAGVNGPLVILDQVKFPRYAEIVHLTLPDGTKRSGQVLEVTGSKAVVQVFEGTSGIDAKKTTCEFTGD 116
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
84-483 |
3.09e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 139.56 E-value: 3.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 84 QVLEVTGSKAVVQVFEGTSGIDAKKTTcEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPAvLAEDYLDIMGQPINPQCRI 163
Cdd:PRK06820 64 EVVSIEQEMALLSPFASSDGLRCGQWV-TPLGHMHQVQVGADLAGRILDGLGAPIDGGPP-LTGQWRELDCPPPSPLTRQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 164 YPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvkkSKDVMdysednfaiVFAAMGvnmETARFF 243
Cdd:PRK06820 142 PIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCADS-----AADVM---------VLALIG---ERGREV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 244 KSDFEENGSMD---NVCLFLNLVNDPTIERIITPRLALTSAEFLAyQCEKHVLVILTDMSSYAEALREVSAAREEVPGRR 320
Cdd:PRK06820 205 REFLEQVLTPEaraRTVVVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 321 GFPGYMYTDLATIYERAGRVEgrNGSITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 400
Cdd:PRK06820 284 SFPPSVFANLPRLLERTGNSD--RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 401 MKSAIGEGmtRKDHSDVSNQLYACYaigKDVQAMKAVvgEEALTSDDLLYLEFLQKFE--RNFISQGAYENRTVFETLDI 478
Cdd:PRK06820 362 MPQIVSAG--QLAMAQKLRRMLACY---QEIELLVRV--GEYQAGEDLQADEALQRYPaiCAFLQQDHSETAHLETTLEH 434
|
....*
gi 33504537 479 GWQLL 483
Cdd:PRK06820 435 LAQVV 439
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
114-404 |
8.63e-36 |
|
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273365 [Multi-domain] Cd Length: 501 Bit Score: 139.45 E-value: 8.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 114 TGDILRTPVSEDMLGRVFNGSGKPID-RGPaVLAEDYLDImgQPINPQC--RIYPEEMIQTGISAIDGMNSIARGQKIPI 190
Cdd:TIGR00962 90 TGRILEVPVGDGLLGRVVNALGEPIDgKGP-IDSDEFSPV--EKIAPGVieRKSVHEPLQTGIKAIDAMIPIGRGQRELI 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 191 FS--AAGlphneiAAQICRQAGLVKKSKDVMdysednfaIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLVNDPTI 268
Cdd:TIGR00962 167 IGdrQTG------KTAVAIDTIINQKDSDVY--------CIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSAS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 269 ERIITPRLALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGR 343
Cdd:TIGR00962 233 LQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAAKLndEKG 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33504537 344 NGSITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 404
Cdd:TIGR00962 309 GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAA 369
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
118-407 |
2.76e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 134.04 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 118 LRTPVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLP 197
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 198 HNEIAAQIcrqaglVKKSKDVMDysednfaiVFAAMGvnmETARFFKSDFEEN--GSMDNVCLFLNLVNDPTIERIITPR 275
Cdd:PRK08472 170 KSTLMGMI------VKGCLAPIK--------VVALIG---ERGREIPEFIEKNlgGDLENTVIVVATSDDSPLMRKYGAF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 276 LALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRnGSITQIPILTM 355
Cdd:PRK08472 233 CAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVLV 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 33504537 356 PNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGE 407
Cdd:PRK08472 311 EGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
84-434 |
1.46e-31 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 126.22 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 84 QVLEVTGSKAVVQVFEGTSGIdakktTCEFTGDILR----TPVSEDMLGRVFNGSGKPID--RGPAVLAEDYlDIMGQPi 157
Cdd:PRK07594 56 EVVGINGSKALLSPFTSTIGL-----HCGQQVMALRrrhqVPVGEALLGRVIDGFGRPLDgrELPDVCWKDY-DAMPPP- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 158 nPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvkkskDVMdysednfaiVFAAMGVNM 237
Cdd:PRK07594 129 -AMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDA-----DSN---------VLVLIGERG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 238 ETARFFkSDFEENGSMDNVCLFLNLVND-PTIERIITPRLALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEV 316
Cdd:PRK07594 194 REVREF-IDFTLSEETRKRCVIVVATSDrPALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGET 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 317 PGRRGFPGYMYTDLATIYERAGRveGRNGSITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPS 396
Cdd:PRK07594 272 AVSGEYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLAT 349
|
330 340 350
....*....|....*....|....*....|....*...
gi 33504537 397 LSRLMKSAIGEgmtrkDHSDVSNQLYACYAIGKDVQAM 434
Cdd:PRK07594 350 LSRVFPVVTSH-----EHRQLAAILRRCLALYQEVELL 382
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
66-464 |
1.45e-30 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 123.73 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 66 RYAEIVHLTLPDGT-KRSGQVLEVTGSKAVVQVFEGTSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPAV 144
Cdd:PRK09099 44 TLGELCELRQRDGTlLQRAEVVGFSRDVALLSPFGELGGL-SRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 145 LAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvkkSKDVMdysed 224
Cdd:PRK09099 123 DCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGT-----QCDVN----- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 225 nfaiVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLVNDPTIERIITPRLALTSAEFLAYQcEKHVLVILTDMSSYAE 304
Cdd:PRK09099 193 ----VIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDR-GLRVLLMMDSLTRFAR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 305 ALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHN 384
Cdd:PRK09099 268 AQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 385 RQIYPPINVLPSLSRLMKSaigegMTRKDHSDVSNQLYACYAIGKDVQAMKAvVGEEALTSDDLLYlEFLQKFE--RNFI 462
Cdd:PRK09099 346 RNQYPAIDVLGSLSRVMPQ-----VVPREHVQAAGRLRQLLAKHREVETLLQ-VGEYRAGSDPVAD-EAIAKIDaiRDFL 418
|
..
gi 33504537 463 SQ 464
Cdd:PRK09099 419 SQ 420
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
117-399 |
1.57e-30 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 119.97 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 117 ILRTPVSEDMLGRVFNGSGKPIDRGPAVLAEDY--LDIMGQPINPQCRIYpeEMIQTGISAIDGMNSIARGQKIPIFSAa 194
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERrrVESKAPGIIPRQSVN--EPLQTGIKAIDSLIPIGRGQRELIIGD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 195 glphneiaaqicRQAGLVKKSKD-VMDYSEDNFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLVNDPTIERIIT 273
Cdd:cd01132 78 ------------RQTGKTAIAIDtIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 274 PRLALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRNGSIT 348
Cdd:cd01132 146 PYAGCAMGEYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGSLT 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 33504537 349 QIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSR 399
Cdd:cd01132 222 ALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
119-487 |
1.77e-29 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 120.66 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 119 RTPVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPH 198
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 199 NEIAAQICR--QAglvkkskDVmdysednfaIVFAAMGvnmETARFFKsDFEEN-----GSMDNVclflnLVNDPTIeri 271
Cdd:PRK07960 189 SVLLGMMARytQA-------DV---------IVVGLIG---ERGREVK-DFIENilgaeGRARSV-----VIAAPAD--- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 272 ITPRLALTSAEFLAYQCE------KHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNG 345
Cdd:PRK07960 241 VSPLLRMQGAAYATRIAEdfrdrgQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 346 SITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSdvSNQLYACY 425
Cdd:PRK07960 321 SITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQ--FKQLLSSF 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33504537 426 AIGKDVQAmkavVGEEALTSDDLL--YLEFLQKFERnFISQGAYEnRTVFEtlDIGWQLLRIFP 487
Cdd:PRK07960 399 QRNRDLVS----VGAYAKGSDPMLdkAIALWPQLEA-FLQQGIFE-RADWE--DSLQALERIFP 454
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
45-464 |
6.23e-29 |
|
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 211621 [Multi-domain] Cd Length: 461 Bit Score: 119.05 E-value: 6.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 45 TYKTVAGVNGPLVildQVKFPRYA--EIVHLTLPDGTKRSGQVLEVT---GSKAVVQVFEGTSGIDAKKTTCEFTGDILR 119
Cdd:TIGR01039 1 TKGKVVQVIGPVV---DVEFEQGElpRIYNALKVQNRAESELTLEVAqhlGDDTVRTIAMGSTDGLVRGLEVIDTGAPIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 120 TPVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGlphn 199
Cdd:TIGR01039 78 VPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAG---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 200 eiaaqicrqaglVKKSKDVMDYSeDNFAI------VFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLVNDPTIERIIT 273
Cdd:TIGR01039 154 ------------VGKTVLIQELI-NNIAKehggysVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 274 PRLALTSAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPIL 353
Cdd:TIGR01039 221 ALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERI--TSTKTGSITSVQAV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 354 TMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMK-SAIGEgmtrkDHSDVSNQLYACYAIGKDVQ 432
Cdd:TIGR01039 299 YVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE-----EHYDVARGVQQILQRYKELQ 373
|
410 420 430
....*....|....*....|....*....|..
gi 33504537 433 AMKAVVGEEALTSDDLLYLEFLQKFERnFISQ 464
Cdd:TIGR01039 374 DIIAILGMDELSEEDKLTVERARRIQR-FLSQ 404
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
116-438 |
1.29e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 117.91 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 116 DILRTPVSEDMLGRVFNGSGKPID-RGPaVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAA 194
Cdd:PRK05688 99 DTGRLPMGMSMLGRVLDGAGRALDgKGP-MKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 195 GLPHNEIAAQICRqaglvkkskdvmdYSEDNFAIVfaamGVNMETARFFKSDFEE---NGSMDNVCLFLNLVNDPTIERI 271
Cdd:PRK05688 178 GVGKSVLLGMMTR-------------FTEADIIVV----GLIGERGREVKEFIEHilgEEGLKRSVVVASPADDAPLMRL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 272 ITPRLALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIP 351
Cdd:PRK05688 241 RAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAFY 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 352 ILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG-EGMTRKDHsdvSNQLYACYAIGKD 430
Cdd:PRK05688 320 TVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDpEHLRRAQR---FKQLWSRYQQSRD 396
|
....*...
gi 33504537 431 VQAMKAVV 438
Cdd:PRK05688 397 LISVGAYV 404
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
114-404 |
2.32e-28 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 117.76 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 114 TGDILRTPVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDI--MGQPINPQCRIYpeEMIQTGISAIDGMNSIARGQKIPIF 191
Cdd:CHL00059 70 TGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIesPAPGIISRRSVY--EPLQTGLIAIDSMIPIGRGQRELII 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 192 SAaglphneiaaqicRQAG---------LVKKSKDVMdysednfaIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNL 262
Cdd:CHL00059 148 GD-------------RQTGktavatdtiLNQKGQNVI--------CVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAET 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 263 VNDPTIERIITPRLALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGR 339
Cdd:CHL00059 207 ADSPATLQYLAPYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAK 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33504537 340 VEGR--NGSITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 404
Cdd:CHL00059 283 LSSQlgEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAA 349
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
45-404 |
2.81e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 117.02 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 45 TYKTVAGVngplvildqVKFPRYAEIVHLTLPDGTKRsGQVLEVTGSKAVVQVFEgtSGIDAKKTTCEFTGDILRTPVSE 124
Cdd:PRK06002 36 SHYRVRGL---------SRFVRLGDFVAIRADGGTHL-GEVVRVDPDGVTVKPFE--PRIEIGLGDAVFRKGPLRIRPDP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 125 DMLGRVFNGSGKPID-RGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAA 203
Cdd:PRK06002 104 SWKGRVINALGEPIDgLGPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 204 QICRQAG-------LV-KKSKDVMDYSEDnfaivfaAMGVNMETARFFKSDFEENGSMdnvclflnlvndptieRIITPR 275
Cdd:PRK06002 184 MLARADAfdtvviaLVgERGREVREFLED-------TLADNLKKAVAVVATSDESPMM----------------RRLAPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 276 LALTSAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTM 355
Cdd:PRK06002 241 TATAIAEYFRDRGEN-VLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLV 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 33504537 356 PNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 404
Cdd:PRK06002 320 DGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
114-399 |
3.44e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 117.32 E-value: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 114 TGDILRTPVSEDMLGRVFNGSGKPIDRGPAVLAEDYLdimgqPINpqcRIYPEEM--------IQTGISAIDGMNSIARG 185
Cdd:PRK13343 91 TGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARR-----PLE---RPAPAIIerdfvtepLQTGIKVVDALIPIGRG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 186 QKIPIFSAAGLPHNEIAAQicrqAGLVKKSKDVMdysednfaIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLVND 265
Cdd:PRK13343 163 QRELIIGDRQTGKTAIAID----AIINQKDSDVI--------CVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 266 PTIERIITPRLALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRN- 344
Cdd:PRK13343 231 PPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELg 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 33504537 345 -GSITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSR 399
Cdd:PRK13343 310 gGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
114-400 |
1.00e-27 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 115.09 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 114 TGDILRTPVSEDMLGRVFNGSGKPIDR---GPAVLAE-DYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIP 189
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGKIVERfdaPPTVGPIsEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 190 IFSAAGLPHNEIAAQICRQA-------GLV-KKSKDVMDYSE--------DNFAIVFAAmgvnmetarffkSDFeengsm 253
Cdd:PRK08149 156 IFASAGCGKTSLMNMLIEHSeadvfviGLIgERGREVTEFVEslrassrrEKCVLVYAT------------SDF------ 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 254 dnvclflnlvndPTIERIITPRLALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATI 333
Cdd:PRK08149 218 ------------SSVDRCNAALVATTVAEYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRL 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33504537 334 YERAGRVegRNGSITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 400
Cdd:PRK08149 285 LERPGAT--LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
112-430 |
6.87e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 112.89 E-value: 6.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 112 EFTGDILRTPVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIF 191
Cdd:PRK07721 85 EATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 192 SAAGLPHNEIAAQICRQAglvkkSKDVMdysednfaiVFAAMGVN-METARFFKSDFEENGSMDNVcLFLNLVNDPTIER 270
Cdd:PRK07721 165 AGSGVGKSTLMGMIARNT-----SADLN---------VIALIGERgREVREFIERDLGPEGLKRSI-VVVATSDQPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 271 IITPRLALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSITQI 350
Cdd:PRK07721 230 IKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNA--SGSITAF 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 351 PILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHSDVSN---QLYACYAI 427
Cdd:PRK07721 307 YTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHKEAANrfrELLSTYQN 381
|
...
gi 33504537 428 GKD 430
Cdd:PRK07721 382 SED 384
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
121-430 |
1.55e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 111.61 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 121 PVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNE 200
Cdd:PRK06793 92 PRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 201 IAAQICRQAglvKKSKDVMDYSEDNfaivfaamgvNMETARFFKSDFEENGsMDNVCLFLNLVNDPTIERIITPRLALTS 280
Cdd:PRK06793 172 LLGMIAKNA---KADINVISLVGER----------GREVKDFIRKELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 281 AEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVP-GRRGFpgYMYTDLATIYERAGRVEgrNGSITQIPILTMPNDD 359
Cdd:PRK06793 238 AEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPiGGKTL--LMESYMKKLLERSGKTQ--KGSITGIYTVLVDGDD 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33504537 360 ITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHSDVSNQLYACYAIGKD 430
Cdd:PRK06793 313 LNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSP-----NHWQLANEMRKILSIYKE 378
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
121-436 |
1.43e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 109.02 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 121 PVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNE 200
Cdd:PRK08972 98 PVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 201 IAAQICRQAglvkkSKDVmdysednfaIVFAAMGvnmETARFFKSDFEE----NGSMDNVCLFLNLVNDPTIeRIITPRL 276
Cdd:PRK08972 178 LLGMMTRGT-----TADV---------IVVGLVG---ERGREVKEFIEEilgeEGRARSVVVAAPADTSPLM-RLKGCET 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 277 ALTSAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMP 356
Cdd:PRK08972 240 ATTIAEYFRDQGLN-VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLTE 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 357 NDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHSDVS---NQLYACYAIGKDVQA 433
Cdd:PRK08972 319 GDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVYSLYQQNRDLIS 393
|
...
gi 33504537 434 MKA 436
Cdd:PRK08972 394 IGA 396
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
77-426 |
2.44e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 102.28 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 77 DGTKRSGQVLEVTGSKAVVQVFEGTSGI--DAKKTTCEFTGDILrtpVSEDMLGRVFNGSGKPID-RGP----AVLAEDY 149
Cdd:PRK07196 48 DETFIEAQVVGFDRDITYLMPFKHPGGVlgGARVFPSEQDGELL---IGDSWLGRVINGLGEPLDgKGQlggsTPLQQQL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 150 ldimgQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRqaglvkkskdvmdYSEDNFAIV 229
Cdd:PRK07196 125 -----PQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITR-------------YTQADVVVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 230 FAAMGVNMETARFFKSDFEENGSMDNVclflnLVNDPTIEriiTPRLALTSAEfLAYQCEKH-------VLVILTDMSSY 302
Cdd:PRK07196 187 GLIGERGREVKEFIEHSLQAAGMAKSV-----VVAAPADE---SPLMRIKATE-LCHAIATYyrdkghdVLLLVDSLTRY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 303 AEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrNGSITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQL 382
Cdd:PRK07196 258 AMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKL 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 33504537 383 HNRQIYPPINVLPSLSRLMKSAIGegmtrKDHSDVSNQLYACYA 426
Cdd:PRK07196 337 AEAGHYPAIDISQSISRCMSQVIG-----SQQAKAASLLKQCYA 375
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
114-399 |
3.92e-23 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 102.45 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 114 TGDILRTPVSEDMLGRVFNGSGKPID-RGPaVLAEDYLD--------IMGQPINpqcriypeEMIQTGISAIDGMNSIAR 184
Cdd:PRK09281 91 TGRILEVPVGEALLGRVVNPLGQPIDgKGP-IEATETRPverkapgvIDRKSVH--------EPLQTGIKAIDAMIPIGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 185 GQKIPIfsaaglphneiaaqIC-RQAG---------LVKKSKDVMdysednfaIVFAAMGVNMETARFFKSDFEENGSMD 254
Cdd:PRK09281 162 GQRELI--------------IGdRQTGktaiaidtiINQKGKDVI--------CIYVAIGQKASTVAQVVRKLEEHGAME 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 255 NVCLFLNLVNDPTIERIITPRLALTSAEFLAYQCeKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLa 331
Cdd:PRK09281 220 YTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNG-KDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL- 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33504537 332 tiYERAGRV--EGRNGSITQIPIL-TMPNDdITRPIPdlTGY--ITEGQIYVDRQLHNRQIYPPINVLPSLSR 399
Cdd:PRK09281 298 --LERAAKLsdELGGGSLTALPIIeTQAGD-VSAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
119-401 |
6.63e-22 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 95.36 E-value: 6.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 119 RTPVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPinpqcriyPE--------EMIQTGISAIDGMNSIARGQKIPI 190
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREA--------PEfvelsteqEILETGIKVVDLLAPYAKGGKIGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 191 FSAAG---------LPHNeiaaqicrqaglVKKSKDVmdYSednfaiVFAAMGvnmETAR--------FFKSDFEENGSM 253
Cdd:cd01133 73 FGGAGvgktvlimeLINN------------IAKAHGG--YS------VFAGVG---ERTRegndlyheMKESGVINLDGL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 254 DNVCLFLNLVNDPTIERIITPRLALTSAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATI 333
Cdd:cd01133 130 SKVALVYGQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSL 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33504537 334 YERAGRVegRNGSITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 401
Cdd:cd01133 210 QERITST--KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
121-399 |
8.58e-22 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 97.67 E-value: 8.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 121 PVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNE 200
Cdd:PRK05922 93 HLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 201 IAAQIcrqaglVKKSKDVMDysednfaiVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLVNDPTIERIITPRLALTS 280
Cdd:PRK05922 173 LLSTI------AKGSKSTIN--------VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 281 AEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSITQI-PILTMPNDd 359
Cdd:PRK05922 239 AEYFRDQGHR-VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILHYPNH- 314
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 33504537 360 itrpiPDL-TGYIT---EGQIYVDRQlHNRQIYPPINVLPSLSR 399
Cdd:PRK05922 315 -----PDIfTDYLKsllDGHFFLTPQ-GKALASPPIDILTSLSR 352
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
114-399 |
9.97e-22 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 98.19 E-value: 9.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 114 TGDILRTPVSEDMLGRVFNGSGKPIDRGPAVLAEDYL-------DIMG-QPINpqcriypeEMIQTGISAIDGMNSIARG 185
Cdd:COG0056 91 TGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRpverpapGVIDrQPVH--------EPLQTGIKAIDAMIPIGRG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 186 QKipifsaaglphnEIaaqIC--RQAG---------LVKKSKDVmdYSednfaiVFAAMGVNMETARFFKSDFEENGSMD 254
Cdd:COG0056 163 QR------------EL---IIgdRQTGktaiaidtiINQKGKDV--IC------IYVAIGQKASTVAQVVETLEEHGAME 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 255 NvCLFlnlV----NDPTIERIITPRLALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMY 327
Cdd:COG0056 220 Y-TIV---VaataSDPAPLQYIAPYAGCAMGEYFMDQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYLH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 328 TDLatiYERAGRV--EGRNGSITQIPIL-TMPNdditrpipDLTGY-------ITEGQIYVDRQLHNRQIYPPINVLPSL 397
Cdd:COG0056 295 SRL---LERAAKLsdELGGGSLTALPIIeTQAG--------DVSAYiptnvisITDGQIFLESDLFNAGIRPAINVGLSV 363
|
..
gi 33504537 398 SR 399
Cdd:COG0056 364 SR 365
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
42-401 |
4.27e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 95.82 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 42 PRLTYKTVAGVNGPLV-ILDQVKFPRYAEIVHLTLPDGTKRSGQVLEVTGSKAVVQVFEGTSGIdAKKTTCEFTGDILRT 120
Cdd:PRK08927 14 TLVIYGRVVAVRGLLVeVAGPIHALSVGARIVVETRGGRPVPCEVVGFRGDRALLMPFGPLEGV-RRGCRAVIANAAAAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 121 PVSEDMLGRVFNGSGKPID-RGPAVLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHN 199
Cdd:PRK08927 93 RPSRAWLGRVVNALGEPIDgKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 200 EIAAQICRQAglvkkSKDVmdysednfaivfAAMGVNMETAR----FFKSDFEENGSMDNVcLFLNLVNDPTIERIITPR 275
Cdd:PRK08927 173 VLLSMLARNA-----DADV------------SVIGLIGERGRevqeFLQDDLGPEGLARSV-VVVATSDEPALMRRQAAY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 276 LALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTM 355
Cdd:PRK08927 235 LTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLFTVLV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 33504537 356 PNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 401
Cdd:PRK08927 314 DGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
123-484 |
1.31e-18 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 88.49 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 123 SEDMLGRVFNGSGKPI-DRGPAVLAEDYLD----IMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIF--SAAG 195
Cdd:PRK07165 76 SKEYFGKIIDIDGNIIyPEAQNPLSKKFLPntssIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIgdRQTG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 196 LPH---NEIAAQicrqaglvkkskdvmdySEDNFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFlNLVNDPTIERII 272
Cdd:PRK07165 156 KTHialNTIINQ-----------------KNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIII-DAPSTSPYEQYL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 273 TPRLALTSAEFLAYqcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNgSITQIPI 352
Cdd:PRK07165 218 APYVAMAHAENISY--NDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRK-TITALPI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 353 LTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRlmksaIGEGMTRKDHSDVS---NQLYACYAIGK 429
Cdd:PRK07165 295 LQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR-----TGSSVQSKTITKVAgeiSKIYRAYKRQL 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 33504537 430 DVQAMKAVVGEEalTSDDLLYLEFLQKFernFISQG--AYENRTVFETLD-IGWQLLR 484
Cdd:PRK07165 370 KLSMLDYDLNKE--TSDLLFKGKMIEKM---FNQKGfsLYSYRFVLLISKlISWGLLK 422
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
126-399 |
5.58e-18 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 84.16 E-value: 5.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 126 MLGRVFNGSGKPIDRgpavLAEDYLDIMGQPINPQC-----------RIYPEEMIQTGISAIDGMNSIARGqkipifSAA 194
Cdd:cd01134 10 LLGSIFDGIQRPLEV----IAETGSIFIPRGVNVQRwpvrqprpvkeKLPPNVPLLTGQRVLDTLFPVAKG------GTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 195 GLPHNEIAAQICRQAGLVKkskdvmdYSEDNfAIVFAAMGVN-METARFFKsDFEE-------NGSMDNVCLFLNLVNDP 266
Cdd:cd01134 80 AIPGPFGCGKTVISQSLSK-------WSNSD-VVIYVGCGERgNEMAEVLE-EFPElkdpitgESLMERTVLIANTSNMP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 267 TIERIITPRLALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE----- 341
Cdd:cd01134 151 VAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRclgsp 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 33504537 342 GRNGSITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSR 399
Cdd:cd01134 230 GREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
48-455 |
2.93e-16 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 81.37 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 48 TVAGVNGPLVILDQVKFPRYAEIVHLtlpDGTKRSGQVLEVTGSKAVVQVFEGTSGIdAKKTTCEFTGDilrtPVSED-- 125
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYEVVRV---GEEGLIGEIIRIEGDKATIQVYEETSGI-KPGEPVEFTGE----PLSVElg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 126 --MLGRVFNG-----------SGKPIDRG---------------PAVLAEDYL---DIMGQ-------------PINPQC 161
Cdd:PRK04192 78 pgLLGSIFDGiqrpldelaekSGDFLERGvyvpaldrekkweftPTVKVGDKVeagDILGTvqetpsiehkimvPPGVSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 162 RI----------------------------------------------YPEEMIQTGISAIDGMNSIARGQK--IPIFSA 193
Cdd:PRK04192 158 TVkeivsegdytvddtiavlededgegveltmmqkwpvrrprpykeklPPVEPLITGQRVIDTFFPVAKGGTaaIPGPFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 194 AG---LPHneiaaQICRQAglvkkSKDVmdysednfaIVFAAMG--VNmETARFFKsDFEE-------NGSMDNVCLFLN 261
Cdd:PRK04192 238 SGktvTQH-----QLAKWA-----DADI---------VIYVGCGerGN-EMTEVLE-EFPElidpktgRPLMERTVLIAN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 262 LVNDPTIER---IITprlALTSAEF---LAYqcekHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYE 335
Cdd:PRK04192 297 TSNMPVAAReasIYT---GITIAEYyrdMGY----DVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 336 RAGRVE---GRNGSITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSrLMKSAIGEGMTRK 412
Cdd:PRK04192 370 RAGRVKtlgGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYS-LYLDQVAPWWEEN 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 33504537 413 DHSDVS---NQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLE--------FLQ 455
Cdd:PRK04192 449 VDPDWRelrDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEvarliredFLQ 502
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
253-398 |
2.79e-15 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 78.91 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 253 MDNVCLFLNLVNDPTIERIITPRLALTSAEF---LAYQcekhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTD 329
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEYfrdMGYD----VALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASK 792
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33504537 330 LATIYERAGRV-----EGRNGSITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLS 398
Cdd:PRK14698 793 LAEFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
114-464 |
3.24e-15 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 77.82 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 114 TGDILRTPVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDIMGQPinpqcriyPE--------EMIQTGISAIDGMNSIARG 185
Cdd:COG0055 75 TGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPA--------PPfeeqstktEILETGIKVIDLLAPYAKG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 186 QKIPIFSAAG---------LPHNeIAAQicrQAGlvkkskdvmdYSednfaiVFAAMGvnmETARF---FKSDFEENGSM 253
Cdd:COG0055 147 GKIGLFGGAGvgktvlimeLIHN-IAKE---HGG----------VS------VFAGVG---ERTREgndLYREMKESGVL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 254 DNVCLFLNLVNDPTIERIITPRLALTSAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATI 333
Cdd:COG0055 204 DKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGAL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 334 YERAGRVegRNGSITQIPILTMPNDDITRPIP-------DLTgyitegqIYVDRQLHNRQIYPPINVLPSLSRLMKSAI- 405
Cdd:COG0055 284 QERITST--KKGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLIv 354
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33504537 406 GEgmtrkDHSDVSN------QLYacyaigKDVQAMKAVVGEEALTSDDLLYLEFLQKFERnFISQ 464
Cdd:COG0055 355 GE-----EHYRVARevqrilQRY------KELQDIIAILGMDELSEEDKLTVARARKIQR-FLSQ 407
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
114-409 |
1.06e-14 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 76.62 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 114 TGDILRTPVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDI--------MGQPiNPQCRIYPEEMIQTGISAIDGMNSIARG 185
Cdd:PTZ00185 111 TGKLLYIPVGAGVLGKVVNPLGHEVPVGLLTRSRALLESeqtlgkvdAGAP-NIVSRSPVNYNLLTGFKAVDTMIPIGRG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 186 QKIPIFSAAGLPHNEIA-AQICRQaglVKKSKDVMdySEDNFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLVN 264
Cdd:PTZ00185 190 QRELIVGDRQTGKTSIAvSTIINQ---VRINQQIL--SKNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 265 DPTIERIITPRLALTSAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE-GR 343
Cdd:PTZ00185 265 EPAGLQYLAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpGK 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33504537 344 NG-SITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 409
Cdd:PTZ00185 344 GGgSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
114-464 |
1.21e-14 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 76.23 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 114 TGDILRTPVSEDMLGRVFNGSGKPIDRGPAVLAEDYLDI-MGQPINPQCRIYPEeMIQTGISAIDGMNSIARGQKIPIFS 192
Cdd:CHL00060 90 TGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIhRSAPAFIQLDTKLS-IFETGIKVVDLLAPYRRGGKIGLFG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 193 AAGlphneiaaqicrqaglVKKSKDVMDYSeDNFA------IVFAAMG--------VNMETaRFFKSDFEENGSMDNVCL 258
Cdd:CHL00060 169 GAG----------------VGKTVLIMELI-NNIAkahggvSVFGGVGertregndLYMEM-KESGVINEQNIAESKVAL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 259 FLNLVNDPTIERIITPRLALTSAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAG 338
Cdd:CHL00060 231 VYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERIT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 339 RVegRNGSITQIPILTMPNDDITRPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHSDV 417
Cdd:CHL00060 311 ST--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIvGE-----EHYET 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 33504537 418 SNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFERnFISQ 464
Cdd:CHL00060 384 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIER-FLSQ 429
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
414-484 |
2.59e-11 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 59.38 E-value: 2.59e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33504537 414 HSDVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFERnFISQGAYENRTVFETLDIGWQLLR 484
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
49-115 |
8.44e-10 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 54.86 E-value: 8.44e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 49 VAGVNGPLVILDQVKFPRYAEIVHLTLP---DGTKRSGQVLEVTGSKAVVQVFEGTSGIDaKKTTCEFTG 115
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVElveFGSLVLGEVLNLGGDKVRVQVFGGTSGLS-RGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
46-116 |
5.45e-09 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 52.70 E-value: 5.45e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33504537 46 YKTVAGVNGPLVILDQVKFPRYAEIVHLTLPDG---TKRSGQVLEVTGSKAVVQVFEGTSGIDaKKTTCEFTGD 116
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGnneTVLKAEVIGFRGDRAILQLFESTRGLS-RGALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
52-139 |
2.99e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 43.47 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 52 VNGPLVILDQVKFPRYAEIVHLtlpDGTKRSGQVLEVTGSKAVVQVFEGTSGIDAKKTTcEFTGDILRTPVSEDMLGRVF 131
Cdd:PRK14698 10 VTGPLVIADGMKGAKMYEVVRV---GELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPV-EGTGSSLSVELGPGLLTSIY 85
|
....*...
gi 33504537 132 NGSGKPID 139
Cdd:PRK14698 86 DGIQRPLE 93
|
|
| ATP-synt_V_A-type_alpha_N |
cd18119 |
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of ... |
48-104 |
1.68e-03 |
|
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349743 [Multi-domain] Cd Length: 67 Bit Score: 37.12 E-value: 1.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504537 48 TVAGVNGPLVILDQVKFPRYAEIV---HLTLPdgtkrsGQVLEVTGSKAVVQVFEGTSGI 104
Cdd:cd18119 3 KIYRVSGPVVVAEGMSGAAMYELVrvgEEGLI------GEIIRLEGDKATIQVYEETSGL 56
|
|
| |
